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Protein

Fructose-1,6-bisphosphatase 1

Gene

FBP1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain (By similarity).By similarity

Catalytic activityi

D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.

Cofactori

Mg2+4 PublicationsNote: Binds 3 Mg2+ ions per subunit.4 Publications

Enzyme regulationi

Subject to complex allosteric regulation. The enzyme can assume an active R-state, or an inactive T-state. Intermediate conformations may exist. AMP acts as allosteric inhibitor. AMP binding affects the turnover of bound substrate and not the affinity for substrate. Fructose 2,6-bisphosphate acts as competitive inhibitor. Fructose 2,6-bisphosphate and AMP have synergistic effects.6 Publications

Kineticsi

  1. KM=1.2 µM for fructose-1,6-diphosphate1 Publication

    Pathway: gluconeogenesis

    This protein is involved in the pathway gluconeogenesis, which is part of Carbohydrate biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway gluconeogenesis and in Carbohydrate biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi69 – 691Magnesium 11 Publication
    Metal bindingi98 – 981Magnesium 11 Publication
    Metal bindingi98 – 981Magnesium 21 Publication
    Metal bindingi119 – 1191Magnesium 21 Publication
    Metal bindingi119 – 1191Magnesium 31 Publication
    Metal bindingi121 – 1211Magnesium 2; via carbonyl oxygen1 Publication
    Metal bindingi122 – 1221Magnesium 31 Publication
    Binding sitei141 – 1411AMP1 Publication
    Binding sitei265 – 2651Substrate
    Metal bindingi281 – 2811Magnesium 31 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi18 – 225AMP1 Publication
    Nucleotide bindingi28 – 325AMP1 Publication
    Nucleotide bindingi113 – 1142AMP1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Gluconeogenesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.1.3.11. 6170.
    SABIO-RKP00636.
    UniPathwayiUPA00138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-1,6-bisphosphatase 1 (EC:3.1.3.11)
    Short name:
    FBPase 1
    Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase 1
    Liver FBPase
    Gene namesi
    Name:FBP1
    Synonyms:FBP
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227 Componenti: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi55 – 551A → L: Destabilizes the inactive T-state and promotes transition to the R-state.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 338337Fructose-1,6-bisphosphatase 1PRO_0000200500Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine2 Publications
    Modified residuei151 – 1511N6-succinyllysineBy similarity
    Modified residuei208 – 2081Phosphoserine; by PKA1 Publication
    Modified residuei216 – 2161PhosphotyrosineBy similarity
    Modified residuei265 – 2651PhosphotyrosineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP00636.
    PRIDEiP00636.

    Expressioni

    Gene expression databases

    GenevisibleiP00636. SS.

    Interactioni

    Subunit structurei

    Homotetramer.9 Publications

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000011671.

    Structurei

    Secondary structure

    1
    338
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 2411Combined sources
    Helixi30 – 5021Combined sources
    Turni51 – 566Combined sources
    Beta strandi59 – 646Combined sources
    Beta strandi66 – 683Combined sources
    Beta strandi70 – 723Combined sources
    Helixi73 – 8816Combined sources
    Beta strandi92 – 976Combined sources
    Beta strandi101 – 1055Combined sources
    Helixi108 – 1103Combined sources
    Beta strandi111 – 12212Combined sources
    Helixi124 – 1263Combined sources
    Turni127 – 1304Combined sources
    Beta strandi133 – 1419Combined sources
    Beta strandi144 – 1463Combined sources
    Beta strandi147 – 1493Combined sources
    Helixi150 – 1534Combined sources
    Helixi157 – 1593Combined sources
    Beta strandi161 – 17818Combined sources
    Beta strandi181 – 1888Combined sources
    Turni189 – 1924Combined sources
    Beta strandi193 – 1986Combined sources
    Beta strandi208 – 2114Combined sources
    Helixi214 – 2196Combined sources
    Helixi222 – 23211Combined sources
    Beta strandi235 – 2373Combined sources
    Beta strandi242 – 2454Combined sources
    Helixi249 – 25911Combined sources
    Beta strandi262 – 2654Combined sources
    Beta strandi268 – 2703Combined sources
    Turni271 – 2733Combined sources
    Beta strandi275 – 2773Combined sources
    Turni278 – 2814Combined sources
    Helixi282 – 29110Combined sources
    Beta strandi295 – 2973Combined sources
    Beta strandi299 – 3024Combined sources
    Helixi303 – 3053Combined sources
    Beta strandi309 – 3124Combined sources
    Beta strandi317 – 3204Combined sources
    Helixi322 – 33413Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CNQX-ray2.27A2-338[»]
    1EYIX-ray2.32A2-338[»]
    1EYJX-ray2.28A/B2-338[»]
    1EYKX-ray2.23A/B2-338[»]
    1FBCX-ray2.60A/B2-336[»]
    1FBDX-ray2.90A/B2-336[»]
    1FBEX-ray3.00A/B2-336[»]
    1FBFX-ray2.70A/B2-336[»]
    1FBGX-ray3.00A/B2-336[»]
    1FBHX-ray2.50A/B2-336[»]
    1FBPX-ray2.50A/B2-336[»]
    1FJ6X-ray2.50A2-338[»]
    1FJ9X-ray2.50A/B2-338[»]
    1FPBX-ray2.60A/B2-336[»]
    1FPDX-ray2.10A/B2-336[»]
    1FPEX-ray2.20A/B2-336[»]
    1FPFX-ray2.10A/B2-336[»]
    1FPGX-ray2.30A/B2-336[»]
    1FPIX-ray2.30A/B2-336[»]
    1FPJX-ray2.20A/B2-336[»]
    1FPKX-ray3.00A/B2-336[»]
    1FPLX-ray2.30A/B2-336[»]
    1FRPX-ray2.00A/B2-336[»]
    1FSAX-ray2.30A/B2-338[»]
    1KZ8X-ray2.00A/F2-338[»]
    1LEVX-ray2.15A/F2-338[»]
    1NUWX-ray1.30A2-338[»]
    1NUXX-ray1.60A2-338[»]
    1NUYX-ray1.30A2-338[»]
    1NUZX-ray1.90A2-338[»]
    1NV0X-ray1.80A2-338[»]
    1NV1X-ray1.90A2-338[»]
    1NV2X-ray2.10A2-338[»]
    1NV3X-ray2.00A2-338[»]
    1NV4X-ray1.90A2-338[»]
    1NV5X-ray1.90A2-338[»]
    1NV6X-ray2.15A2-338[»]
    1NV7X-ray2.15A/B2-338[»]
    1Q9DX-ray2.35A/B2-338[»]
    1RDXX-ray2.75A/B2-338[»]
    1RDYX-ray2.20A/B2-338[»]
    1RDZX-ray2.05A/B2-338[»]
    1YXIX-ray2.00A2-338[»]
    1YYZX-ray1.85A2-338[»]
    1YZ0X-ray2.07A/B2-338[»]
    2F3BX-ray1.80A1-338[»]
    2F3DX-ray1.83A1-338[»]
    2FBPX-ray2.80A/B2-336[»]
    2QVUX-ray1.50A/B2-338[»]
    2QVVX-ray2.03A/B2-338[»]
    3FBPX-ray2.80A/B2-336[»]
    4FBPX-ray2.50A/B/C/D2-336[»]
    4GBVX-ray2.90A2-336[»]
    4GBWX-ray2.00A2-336[»]
    4GWSX-ray2.75A/B2-338[»]
    4GWUX-ray3.00A2-338[»]
    4GWWX-ray3.20A2-338[»]
    4GWXX-ray2.35A2-338[»]
    4GWYX-ray3.00A2-338[»]
    4GWZX-ray2.60A/B2-338[»]
    4GX3X-ray2.25A/B2-338[»]
    4GX4X-ray2.50A/B2-338[»]
    4GX6X-ray2.50A/B2-338[»]
    4H45X-ray3.10A2-338[»]
    4H46X-ray2.50A2-338[»]
    4KXPX-ray2.70A/B1-338[»]
    5FBPX-ray2.10A/B2-336[»]
    ProteinModelPortaliP00636.
    SMRiP00636. Positions 7-338.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00636.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni122 – 1254Substrate binding
    Regioni213 – 2164Substrate binding
    Regioni244 – 2496Substrate binding
    Regioni275 – 2773Substrate binding

    Sequence similaritiesi

    Belongs to the FBPase class 1 family.Curated

    Phylogenomic databases

    eggNOGiCOG0158.
    HOGENOMiHOG000191265.
    HOVERGENiHBG005627.
    InParanoidiP00636.
    KOiK03841.

    Family and domain databases

    HAMAPiMF_01855. FBPase_class1.
    InterProiIPR000146. FBPase_class-1/SBPase.
    IPR028343. FBPtase.
    IPR020548. Fructose_bisphosphatase_AS.
    [Graphical view]
    PANTHERiPTHR11556. PTHR11556. 1 hit.
    PfamiPF00316. FBPase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500210. FBPtase. 1 hit.
    PIRSF000904. FBPtase_SBPase. 1 hit.
    PRINTSiPR00115. F16BPHPHTASE.
    PROSITEiPS00124. FBPASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00636-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTDQAAFDTN IVTLTRFVME EGRKARGTGE MTQLLNSLCT AVKAISTAVR
    60 70 80 90 100
    KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVINVLKSSF ATCVLVSEED
    110 120 130 140 150
    KNAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSIGTIFGIY RKNSTDEPSE
    160 170 180 190 200
    KDALQPGRNL VAAGYALYGS ATMLVLAMVN GVNCFMLDPA IGEFILVDRD
    210 220 230 240 250
    VKIKKKGSIY SINEGYAKEF DPAITEYIQR KKFPPDNSAP YGARYVGSMV
    260 270 280 290 300
    ADVHRTLVYG GIFMYPANKK SPKGKLRLLY ECNPMAYVME KAGGLATTGK
    310 320 330
    EAVLDIVPTD IHQRAPIILG SPEDVTELLE IYQKHAAK
    Length:338
    Mass (Da):36,779
    Last modified:January 23, 2007 - v4
    Checksum:i610BF8D3C6D320F6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21T → A AA sequence (PubMed:6291465).Curated
    Sequence conflicti4 – 41Q → E AA sequence (PubMed:6291465).Curated
    Sequence conflicti21 – 211E → Q AA sequence (PubMed:6296821).Curated
    Sequence conflicti97 – 971S → T AA sequence (PubMed:6296821).Curated
    Sequence conflicti157 – 1571G → E AA sequence (PubMed:6296821).Curated
    Sequence conflicti200 – 2001D → N AA sequence (PubMed:6296821).Curated
    Sequence conflicti229 – 2291Q → E AA sequence (PubMed:6296821).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M86347 mRNA. Translation: AAA31035.1.
    PIRiS37696. PAPGF.
    RefSeqiNP_999144.1. NM_213979.1.
    UniGeneiSsc.5127.

    Genome annotation databases

    GeneIDi397038.
    KEGGissc:397038.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M86347 mRNA. Translation: AAA31035.1.
    PIRiS37696. PAPGF.
    RefSeqiNP_999144.1. NM_213979.1.
    UniGeneiSsc.5127.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CNQX-ray2.27A2-338[»]
    1EYIX-ray2.32A2-338[»]
    1EYJX-ray2.28A/B2-338[»]
    1EYKX-ray2.23A/B2-338[»]
    1FBCX-ray2.60A/B2-336[»]
    1FBDX-ray2.90A/B2-336[»]
    1FBEX-ray3.00A/B2-336[»]
    1FBFX-ray2.70A/B2-336[»]
    1FBGX-ray3.00A/B2-336[»]
    1FBHX-ray2.50A/B2-336[»]
    1FBPX-ray2.50A/B2-336[»]
    1FJ6X-ray2.50A2-338[»]
    1FJ9X-ray2.50A/B2-338[»]
    1FPBX-ray2.60A/B2-336[»]
    1FPDX-ray2.10A/B2-336[»]
    1FPEX-ray2.20A/B2-336[»]
    1FPFX-ray2.10A/B2-336[»]
    1FPGX-ray2.30A/B2-336[»]
    1FPIX-ray2.30A/B2-336[»]
    1FPJX-ray2.20A/B2-336[»]
    1FPKX-ray3.00A/B2-336[»]
    1FPLX-ray2.30A/B2-336[»]
    1FRPX-ray2.00A/B2-336[»]
    1FSAX-ray2.30A/B2-338[»]
    1KZ8X-ray2.00A/F2-338[»]
    1LEVX-ray2.15A/F2-338[»]
    1NUWX-ray1.30A2-338[»]
    1NUXX-ray1.60A2-338[»]
    1NUYX-ray1.30A2-338[»]
    1NUZX-ray1.90A2-338[»]
    1NV0X-ray1.80A2-338[»]
    1NV1X-ray1.90A2-338[»]
    1NV2X-ray2.10A2-338[»]
    1NV3X-ray2.00A2-338[»]
    1NV4X-ray1.90A2-338[»]
    1NV5X-ray1.90A2-338[»]
    1NV6X-ray2.15A2-338[»]
    1NV7X-ray2.15A/B2-338[»]
    1Q9DX-ray2.35A/B2-338[»]
    1RDXX-ray2.75A/B2-338[»]
    1RDYX-ray2.20A/B2-338[»]
    1RDZX-ray2.05A/B2-338[»]
    1YXIX-ray2.00A2-338[»]
    1YYZX-ray1.85A2-338[»]
    1YZ0X-ray2.07A/B2-338[»]
    2F3BX-ray1.80A1-338[»]
    2F3DX-ray1.83A1-338[»]
    2FBPX-ray2.80A/B2-336[»]
    2QVUX-ray1.50A/B2-338[»]
    2QVVX-ray2.03A/B2-338[»]
    3FBPX-ray2.80A/B2-336[»]
    4FBPX-ray2.50A/B/C/D2-336[»]
    4GBVX-ray2.90A2-336[»]
    4GBWX-ray2.00A2-336[»]
    4GWSX-ray2.75A/B2-338[»]
    4GWUX-ray3.00A2-338[»]
    4GWWX-ray3.20A2-338[»]
    4GWXX-ray2.35A2-338[»]
    4GWYX-ray3.00A2-338[»]
    4GWZX-ray2.60A/B2-338[»]
    4GX3X-ray2.25A/B2-338[»]
    4GX4X-ray2.50A/B2-338[»]
    4GX6X-ray2.50A/B2-338[»]
    4H45X-ray3.10A2-338[»]
    4H46X-ray2.50A2-338[»]
    4KXPX-ray2.70A/B1-338[»]
    5FBPX-ray2.10A/B2-336[»]
    ProteinModelPortaliP00636.
    SMRiP00636. Positions 7-338.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000011671.

    Chemistry

    BindingDBiP00636.
    ChEMBLiCHEMBL2263.

    Proteomic databases

    PaxDbiP00636.
    PRIDEiP00636.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi397038.
    KEGGissc:397038.

    Organism-specific databases

    CTDi2203.

    Phylogenomic databases

    eggNOGiCOG0158.
    HOGENOMiHOG000191265.
    HOVERGENiHBG005627.
    InParanoidiP00636.
    KOiK03841.

    Enzyme and pathway databases

    UniPathwayiUPA00138.
    BRENDAi3.1.3.11. 6170.
    SABIO-RKP00636.

    Miscellaneous databases

    EvolutionaryTraceiP00636.
    PROiP00636.

    Gene expression databases

    GenevisibleiP00636. SS.

    Family and domain databases

    HAMAPiMF_01855. FBPase_class1.
    InterProiIPR000146. FBPase_class-1/SBPase.
    IPR028343. FBPtase.
    IPR020548. Fructose_bisphosphatase_AS.
    [Graphical view]
    PANTHERiPTHR11556. PTHR11556. 1 hit.
    PfamiPF00316. FBPase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500210. FBPtase. 1 hit.
    PIRSF000904. FBPtase_SBPase. 1 hit.
    PRINTSiPR00115. F16BPHPHTASE.
    PROSITEiPS00124. FBPASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Isolation and sequence analysis of the cDNA for pig kidney fructose 1,6-bisphosphatase."
      Williams M.K., Kantrowitz E.R.
      Proc. Natl. Acad. Sci. U.S.A. 89:3080-3082(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    2. "Complete amino acid sequence of pig kidney fructose-1,6-bisphosphatase."
      Marcus F., Edelstein I., Reardon I., Heinrikson R.L.
      Proc. Natl. Acad. Sci. U.S.A. 79:7161-7165(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-336, ACETYLATION AT THR-2, PHOSPHORYLATION AT SER-208.
      Tissue: Kidney cortex.
    3. "Conservation of primary structure at the proteinase-sensitive site of fructose 1,6-bisphosphatases."
      McGregor J.S., Hannappel E., Xu G.-J., Pontremoli S., Horecker B.L.
      Arch. Biochem. Biophys. 217:652-664(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-24 AND 44-61, ACETYLATION AT THR-2.
      Tissue: Kidney.
    4. "Mechanism of action of fructose 1,6-bisphosphatase."
      Benkovic S.J., Demaine M.M.
      Adv. Enzymol. Relat. Areas Mol. Biol. 53:45-82(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE-BINDING SITE, LIGANDS, REVIEW.
    5. "Structure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex at 2.8-A resolution."
      Ke H.M., Thorpe C.M., Seaton B.A., Lipscomb W.N., Marcus F.
      J. Mol. Biol. 212:513-539(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-2,6-BISPHOSPHATE, SEQUENCE REVISION.
    6. "Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium."
      Ke H.M., Zhang Y.P., Lipscomb W.N.
      Proc. Natl. Acad. Sci. U.S.A. 87:5243-5247(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-6-PHOSPHATE; AMP AND MAGNESIUM, ENZYME REGULATION, SUBUNIT.
    7. "Crystal structure of the neutral form of fructose-1,6-bisphosphatase complexed with the product fructose 6-phosphate at 2.1-A resolution."
      Ke H.M., Zhang Y.P., Liang J.-Y., Lipscomb W.N.
      Proc. Natl. Acad. Sci. U.S.A. 88:2989-2993(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-6-PHOSPHATE.
    8. "Crystal structure of the neutral form of fructose 1,6-bisphosphatase complexed with regulatory inhibitor fructose 2,6-bisphosphate at 2.6-A resolution."
      Liang J.-Y., Huang S., Zhang Y.P., Ke H.M., Lipscomb W.N.
      Proc. Natl. Acad. Sci. U.S.A. 89:2404-2408(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-2,6-BISPHOSPHATE.
    9. "Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase."
      Choe J.-Y., Poland B.W., Fromm H.J., Honzatko R.B.
      Biochemistry 37:11441-11450(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) IN COMPLEX WITH ZINC IONS, COFACTOR, ENZYME REGULATION.
    10. "Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes."
      Choe J.-Y., Fromm H.J., Honzatko R.B.
      Biochemistry 39:8565-8574(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) IN COMPLEXES WITH FRUCTOSE-6-PHOSPHATE; PHOSPHATE; AMP; MAGNESIUM AND ZINC IONS, SUBUNIT, ENZYME REGULATION.
    11. "Metaphosphate in the active site of fructose-1,6-bisphosphatase."
      Choe J.-Y., Iancu C.V., Fromm H.J., Honzatko R.B.
      J. Biol. Chem. 278:16015-16020(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM IONS; FRUCTOSE-6-PHOSPHATE AND PHOSPHATE, COFACTOR, ENZYME MECHANISM.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH THE SYNTHETIC INHIBITOR OC252; FRUCTOSE-6-PHOSPHATE; PHOSPHATE AND DIVALENT METAL CATIONS, COFACTOR, SUBUNIT, ENZYME REGULATION.
    13. "R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase."
      Iancu C.V., Mukund S., Fromm H.J., Honzatko R.B.
      J. Biol. Chem. 280:19737-19745(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT LEU-55 IN COMPLEXES WITH AMP; FRUCTORSE-6-PHOSPHAT; PHOSPHATE AND MAGNESIUM IONS, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    14. "Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition."
      Hines J.K., Chen X., Nix J.C., Fromm H.J., Honzatko R.B.
      J. Biol. Chem. 282:36121-36131(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM IONS AND FRUCTOSE-2,6-DIPHOSPHATE, SUBUNIT, ENZYME REGULATION.

    Entry informationi

    Entry nameiF16P1_PIG
    AccessioniPrimary (citable) accession number: P00636
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: June 24, 2015
    This is version 140 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The molecule has a highly reactive cysteine residue (Cys-117 or Cys-129), which tends to form mixed disulfides (e.g. with homocystine) but is not essential for enzyme activity.

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.